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Protein

Sarcoplasmic/endoplasmic reticulum calcium ATPase 2

Gene

ATP2A2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Isoform 2 is involved in the regulation of the contraction/relaxation cycle.1 Publication

Catalytic activityi

ATP + H2O + Ca2+(Side 1) = ADP + phosphate + Ca2+(Side 2).

Enzyme regulationi

Reversibly inhibited by phospholamban (PLN) at low calcium concentrations. Dephosphorylated PLN decreases the apparent affinity of the ATPase for calcium. This inhibition is regulated by the phosphorylation of PLN (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi304 – 3041Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi305 – 3051Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi307 – 3071Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi309 – 3091Calcium 2By similarity
Active sitei351 – 35114-aspartylphosphate intermediateBy similarity
Metal bindingi702 – 7021MagnesiumBy similarity
Metal bindingi706 – 7061MagnesiumBy similarity
Metal bindingi767 – 7671Calcium 1By similarity
Metal bindingi770 – 7701Calcium 1By similarity
Metal bindingi795 – 7951Calcium 2By similarity
Metal bindingi798 – 7981Calcium 1By similarity
Metal bindingi799 – 7991Calcium 1By similarity
Metal bindingi799 – 7991Calcium 2By similarity
Metal bindingi907 – 9071Calcium 1By similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calcium ion binding Source: BHF-UCL
  • calcium-transporting ATPase activity Source: BHF-UCL
  • calcium-transporting ATPase activity involved in regulation of cardiac muscle cell membrane potential Source: BHF-UCL
  • enzyme binding Source: BHF-UCL
  • protein C-terminus binding Source: UniProtKB
  • S100 protein binding Source: UniProtKB

GO - Biological processi

  • blood coagulation Source: Reactome
  • calcium ion import into sarcoplasmic reticulum Source: BHF-UCL
  • calcium ion transmembrane transport Source: BHF-UCL
  • calcium ion transport from cytosol to endoplasmic reticulum Source: BHF-UCL
  • cell adhesion Source: ProtInc
  • cellular calcium ion homeostasis Source: BHF-UCL
  • endoplasmic reticulum calcium ion homeostasis Source: BHF-UCL
  • epidermis development Source: ProtInc
  • ER-nucleus signaling pathway Source: Ensembl
  • ion transmembrane transport Source: Reactome
  • negative regulation of heart contraction Source: Ensembl
  • positive regulation of endoplasmic reticulum calcium ion concentration Source: BHF-UCL
  • positive regulation of heart rate Source: BHF-UCL
  • regulation of cardiac muscle cell action potential involved in regulation of contraction Source: BHF-UCL
  • regulation of cardiac muscle cell membrane potential Source: BHF-UCL
  • regulation of cardiac muscle contraction by calcium ion signaling Source: BHF-UCL
  • regulation of the force of heart contraction Source: Ensembl
  • relaxation of cardiac muscle Source: BHF-UCL
  • response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
  • sarcoplasmic reticulum calcium ion transport Source: BHF-UCL
  • transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Calcium, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_118798. Pre-NOTCH Processing in Golgi.
REACT_23765. Reduction of cytosolic Ca++ levels.
REACT_25149. Ion transport by P-type ATPases.
SignaLinkiP16615.

Protein family/group databases

TCDBi3.A.3.2.7. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (EC:3.6.3.8)
Short name:
SERCA2
Short name:
SR Ca(2+)-ATPase 2
Alternative name(s):
Calcium pump 2
Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform
Endoplasmic reticulum class 1/2 Ca(2+) ATPase
Gene namesi
Name:ATP2A2
Synonyms:ATP2B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:812. ATP2A2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4848CytoplasmicBy similarityAdd
BLAST
Transmembranei49 – 6921Helical; Name=1By similarityAdd
BLAST
Topological domaini70 – 8920LumenalBy similarityAdd
BLAST
Transmembranei90 – 11021Helical; Name=2By similarityAdd
BLAST
Topological domaini111 – 253143CytoplasmicBy similarityAdd
BLAST
Transmembranei254 – 27320Helical; Name=3By similarityAdd
BLAST
Topological domaini274 – 29522LumenalBy similarityAdd
BLAST
Transmembranei296 – 31318Helical; Name=4By similarityAdd
BLAST
Topological domaini314 – 756443CytoplasmicBy similarityAdd
BLAST
Transmembranei757 – 77620Helical; Name=5By similarityAdd
BLAST
Topological domaini777 – 78610LumenalBy similarity
Transmembranei787 – 80721Helical; Name=6By similarityAdd
BLAST
Topological domaini808 – 82720CytoplasmicBy similarityAdd
BLAST
Transmembranei828 – 85023Helical; Name=7By similarityAdd
BLAST
Topological domaini851 – 89646LumenalBy similarityAdd
BLAST
Transmembranei897 – 91620Helical; Name=8By similarityAdd
BLAST
Topological domaini917 – 92913CytoplasmicBy similarityAdd
BLAST
Transmembranei930 – 94819Helical; Name=9By similarityAdd
BLAST
Topological domaini949 – 96315LumenalBy similarityAdd
BLAST
Transmembranei964 – 98421Helical; Name=10By similarityAdd
BLAST
Topological domaini985 – 104258CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  • calcium ion-transporting ATPase complex Source: BHF-UCL
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB
  • integral component of plasma membrane Source: ProtInc
  • longitudinal sarcoplasmic reticulum Source: BHF-UCL
  • membrane Source: MGI
  • platelet dense tubular network membrane Source: Reactome
  • sarcoplasmic reticulum Source: BHF-UCL
  • sarcoplasmic reticulum membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Sarcoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Acrokeratosis verruciformis (AKV)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA localized disorder of keratinization, which is inherited as an autosomal dominant trait. Its onset is early in life with multiple flat-topped, flesh-colored papules on the hands and feet, punctate keratoses on the palms and soles, with varying degrees of nail involvement. The histopathology shows a distinctive pattern of epidermal features with hyperkeratosis, hypergranulosis and acanthosis together with papillomatosis. These changes are frequently associated with circumscribed elevations of the epidermis that are said to resemble church spires. There are no features of dyskeratosis or acantholysis, the typical findings in lesions of Darier disease.

See also OMIM:101900
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti602 – 6021P → L in AKV; loss of activity. 1 Publication
VAR_017532
Darier disease (DD)5 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA skin disorder characterized by warty papules and plaques in seborrheic areas (central trunk, flexures, scalp and forehead), palmoplantar pits and distinctive nail abnormalities. It is due to loss of adhesion between epidermal cells (acantholysis) and abnormal keratinization. Patients with mild disease may have no more than a few scattered keratotic papules or subtle nail changes, whereas those with severe disease are handicapped by widespread malodorous keratotic plaques. Some patients present with hemorrhage into acantholytic vesicles on the palms and dorsal aspects of the fingers which gives rise to black macules. In a few families affected by Darier disease, neuropsychiatric abnormalities such as mild mental retardation, schizophrenia, bipolar disorder and epilepsy have been reported. Stress, UV exposure, heat, sweat, friction and oral contraception exacerbate disease symptoms. Clinical variants of Darier disease include hypertrophic, vesicobullous, hypopigmented, cornifying, zosteriform or linear, acute and comedonal subtypes. Comedonal Darier disease is characterized by the coexistence of acne-like comedonal lesions with typical Darier hyperkeratotic papules on light-exposed areas. At histopathologic level, comedonal Darier disease differs from classic Darier disease in the prominent follicular involvement and the presence of greatly elongated dermal villi.

See also OMIM:124200
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231G → E in DD. 1 Publication
Corresponds to variant rs28929478 [ dbSNP | Ensembl ].
VAR_008608
Natural varianti39 – 391N → T in DD. 1 Publication
VAR_008609
Natural varianti41 – 411Missing in DD; comedonal type. 1 Publication
VAR_063398
Natural varianti47 – 471K → KMFLTGK in DD.
VAR_008610
Natural varianti65 – 651L → S in DD; severe form.
VAR_008611
Natural varianti131 – 1311R → Q in DD.
VAR_008612
Natural varianti160 – 1601P → L in DD.
VAR_008613
Natural varianti186 – 1861S → P in DD.
VAR_008614
Natural varianti211 – 2111G → D in DD; severe form.
VAR_008615
Natural varianti223 – 2231V → M in DD.
VAR_008616
Natural varianti268 – 2681C → F in DD; haemorrhagic lesions.
VAR_008617
Natural varianti310 – 3101G → V in DD.
VAR_008618
Natural varianti318 – 3181C → R in DD; severe form.
VAR_008619
Natural varianti348 – 3481I → T in DD.
VAR_008620
Natural varianti357 – 3571T → K in DD. 1 Publication
VAR_009508
Natural varianti412 – 4121E → G in DD.
VAR_008621
Natural varianti495 – 4951S → F in DD. 1 Publication
VAR_008622
Natural varianti560 – 5601C → R in DD; neuropsychiatric phenotype. 1 Publication
VAR_008623
Natural varianti675 – 6751F → S in DD; multiple neuropsychiatric features.
VAR_008624
Natural varianti683 – 6831K → E in DD; depression.
VAR_008625
Natural varianti702 – 7021D → N in DD; moderate form.
VAR_008626
Natural varianti745 – 7451A → D in DD; moderate form.
VAR_008627
Natural varianti749 – 7491G → R in DD. 1 Publication
VAR_009509
Natural varianti754 – 7541Missing in DD.
VAR_008628
Natural varianti765 – 7651S → L in DD. 1 Publication
VAR_008629
Natural varianti767 – 7671N → S in DD; haemorrhagic lesions and neuropsychiatric phenotype.
VAR_008630
Natural varianti769 – 7691G → R in DD.
VAR_008631
Natural varianti803 – 8031A → T in DD; mild/moderate form.
VAR_008632
Natural varianti838 – 8381A → P in DD; severe form; petit mal epilepsy.
VAR_008633
Natural varianti843 – 8431V → F in DD; depression.
VAR_008634
Natural varianti875 – 8751C → G in DD; retinitis pigmentosa.
VAR_008635
Natural varianti920 – 9201S → Y in DD; mild/moderate/severe form; one patient with epilepsy.
VAR_008636
Natural varianti943 – 9431H → R in DD; learning difficulties.
VAR_008637
Natural varianti975 – 9751P → R in DD.
VAR_008638

Keywords - Diseasei

Disease mutation, Epilepsy

Organism-specific databases

MIMi101900. phenotype.
124200. phenotype.
Orphaneti79151. Acrokeratosis verruciformis of Hopf.
218. Darier disease.
PharmGKBiPA71.

Polymorphism and mutation databases

BioMutaiATP2A2.
DMDMi114312.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10421042Sarcoplasmic/endoplasmic reticulum calcium ATPase 2PRO_0000046196Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki143 – 143Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei294 – 2941Nitrated tyrosine1 Publication
Modified residuei295 – 2951Nitrated tyrosine1 Publication
Modified residuei580 – 5801Phosphoserine1 Publication
Modified residuei663 – 6631Phosphoserine4 Publications

Post-translational modificationi

Nitrated under oxidative stress. Nitration on the two tyrosine residues inhibits catalytic activity.1 Publication

Keywords - PTMi

Isopeptide bond, Nitration, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP16615.
PaxDbiP16615.
PRIDEiP16615.

PTM databases

PhosphoSiteiP16615.

Expressioni

Tissue specificityi

Isoform 1 is widely expressed in smooth muscle and nonmuscle tissues such as in adult skin epidermis, with highest expression in liver, pancreas and lung, and intermediate expression in brain, kidney and placenta. Also expressed at lower levels in heart and skeletal muscle. Isoforms 2 and 3 are highly expressed in the heart and slow twitch skeletal muscle. Expression of isoform 3 is predominantly restricted to cardiomyocytes and in close proximity to the sarcolemma. Both isoforms are mildly expressed in lung, kidney, liver, pancreas and placenta. Expression of isoform 3 is amplified during monocytic differentiation and also observed in the fetal heart.3 Publications

Gene expression databases

BgeeiP16615.
CleanExiHS_ATP2A2.
ExpressionAtlasiP16615. baseline and differential.
GenevisibleiP16615. HS.

Organism-specific databases

HPAiHPA062605.

Interactioni

Subunit structurei

Associated with phospholamban (PLN) (By similarity). Isoform 1 interacts with TRAM2 (via C-terminus). Interacts with HAX1. Interacts with S100A8 and S100A9 (By similarity). Interacts with SLC35G1 and STIM1.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
OPRD1P411433EBI-358933,EBI-2624456

Protein-protein interaction databases

BioGridi106978. 45 interactions.
IntActiP16615. 19 interactions.
MINTiMINT-4991144.
STRINGi9606.ENSP00000440045.

Structurei

3D structure databases

ProteinModelPortaliP16615.
SMRiP16615. Positions 1-992.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni370 – 40031Interacts with phospholamban 1By similarityAdd
BLAST
Regioni575 – 59420Interacts with HAX1Add
BLAST
Regioni787 – 80721Interacts with phospholamban 2By similarityAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00760000119003.
HOGENOMiHOG000265621.
HOVERGENiHBG105648.
InParanoidiP16615.
KOiK05853.
OMAiPKESRDN.
OrthoDBiEOG73Z2SF.
PhylomeDBiP16615.
TreeFamiTF300651.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR005782. P-type_ATPase_IIA.
IPR001757. P_typ_ATPase.
IPR030327. SERCA2.
[Graphical view]
PANTHERiPTHR24093:SF234. PTHR24093:SF234. 1 hit.
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
PR00120. HATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01116. ATPase-IIA1_Ca. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Note: SERCA2 transcripts differ only in their 3'-UTR region and are expressed in a tissue-specific manner.

Isoform 1 (identifier: P16615-1) [UniParc]FASTAAdd to basket

Also known as: ATP2A2B, Class 2-4, HK1, SERCA2b

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MENAHTKTVE EVLGHFGVNE STGLSLEQVK KLKERWGSNE LPAEEGKTLL
60 70 80 90 100
ELVIEQFEDL LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILVA
110 120 130 140 150
NAIVGVWQER NAENAIEALK EYEPEMGKVY RQDRKSVQRI KAKDIVPGDI
160 170 180 190 200
VEIAVGDKVP ADIRLTSIKS TTLRVDQSIL TGESVSVIKH TDPVPDPRAV
210 220 230 240 250
NQDKKNMLFS GTNIAAGKAM GVVVATGVNT EIGKIRDEMV ATEQERTPLQ
260 270 280 290 300
QKLDEFGEQL SKVISLICIA VWIINIGHFN DPVHGGSWIR GAIYYFKIAV
310 320 330 340 350
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS
360 370 380 390 400
DKTGTLTTNQ MSVCRMFILD RVEGDTCSLN EFTITGSTYA PIGEVHKDDK
410 420 430 440 450
PVNCHQYDGL VELATICALC NDSALDYNEA KGVYEKVGEA TETALTCLVE
460 470 480 490 500
KMNVFDTELK GLSKIERANA CNSVIKQLMK KEFTLEFSRD RKSMSVYCTP
510 520 530 540 550
NKPSRTSMSK MFVKGAPEGV IDRCTHIRVG STKVPMTSGV KQKIMSVIRE
560 570 580 590 600
WGSGSDTLRC LALATHDNPL RREEMHLEDS ANFIKYETNL TFVGCVGMLD
610 620 630 640 650
PPRIEVASSV KLCRQAGIRV IMITGDNKGT AVAICRRIGI FGQDEDVTSK
660 670 680 690 700
AFTGREFDEL NPSAQRDACL NARCFARVEP SHKSKIVEFL QSFDEITAMT
710 720 730 740 750
GDGVNDAPAL KKAEIGIAMG SGTAVAKTAS EMVLADDNFS TIVAAVEEGR
760 770 780 790 800
AIYNNMKQFI RYLISSNVGE VVCIFLTAAL GFPEALIPVQ LLWVNLVTDG
810 820 830 840 850
LPATALGFNP PDLDIMNKPP RNPKEPLISG WLFFRYLAIG CYVGAATVGA
860 870 880 890 900
AAWWFIAADG GPRVSFYQLS HFLQCKEDNP DFEGVDCAIF ESPYPMTMAL
910 920 930 940 950
SVLVTIEMCN ALNSLSENQS LLRMPPWENI WLVGSICLSM SLHFLILYVE
960 970 980 990 1000
PLPLIFQITP LNVTQWLMVL KISLPVILMD ETLKFVARNY LEPGKECVQP
1010 1020 1030 1040
ATKSCSFSAC TDGISWPFVL LIMPLVIWVY STDTNFSDMF WS
Note: Ubiquitous housekeeping isoform.
Length:1,042
Mass (Da):114,757
Last modified:August 1, 1990 - v1
Checksum:i5462FF2DA7FB630A
GO
Isoform 2 (identifier: P16615-2) [UniParc]FASTAAdd to basket

Also known as: ATP2A2A, Class 1, HK2, SERCA2a

The sequence of this isoform differs from the canonical sequence as follows:
     994-1042: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → AILE

Note: Cardiac/slow twitch, muscle specific isoform. Has a lower affinity for calcium and a higher catalytic turnover rate.
Show »
Length:997
Mass (Da):109,691
Checksum:iDD57D12A2B24FEC1
GO
Isoform 3 (identifier: P16615-3) [UniParc]FASTAAdd to basket

Also known as: SERCA2C

The sequence of this isoform differs from the canonical sequence as follows:
     994-1042: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → VLSSEL

Note: May be due to intron retention. Shows a lower apparent affinity for cytosolic calcium than isoform 2 and a catalytic turnover rate similar to isoform 1.
Show »
Length:999
Mass (Da):109,893
Checksum:iF6BE03E546453B24
GO
Isoform 4 (identifier: P16615-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     155-181: Missing.

Note: No experimental confirmation available.
Show »
Length:1,015
Mass (Da):111,847
Checksum:i6C99B5C382834A63
GO
Isoform 5 (identifier: P16615-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     994-1042: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → DIIK

Note: No experimental confirmation available.
Show »
Length:997
Mass (Da):109,734
Checksum:iD570A12D5B24FEC1
GO

Sequence cautioni

The sequence BAG57266.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231G → E in DD. 1 Publication
Corresponds to variant rs28929478 [ dbSNP | Ensembl ].
VAR_008608
Natural varianti39 – 391N → T in DD. 1 Publication
VAR_008609
Natural varianti41 – 411Missing in DD; comedonal type. 1 Publication
VAR_063398
Natural varianti47 – 471K → KMFLTGK in DD.
VAR_008610
Natural varianti65 – 651L → S in DD; severe form.
VAR_008611
Natural varianti131 – 1311R → Q in DD.
VAR_008612
Natural varianti160 – 1601P → L in DD.
VAR_008613
Natural varianti186 – 1861S → P in DD.
VAR_008614
Natural varianti211 – 2111G → D in DD; severe form.
VAR_008615
Natural varianti223 – 2231V → M in DD.
VAR_008616
Natural varianti268 – 2681C → F in DD; haemorrhagic lesions.
VAR_008617
Natural varianti310 – 3101G → V in DD.
VAR_008618
Natural varianti318 – 3181C → R in DD; severe form.
VAR_008619
Natural varianti348 – 3481I → T in DD.
VAR_008620
Natural varianti357 – 3571T → K in DD. 1 Publication
VAR_009508
Natural varianti412 – 4121E → G in DD.
VAR_008621
Natural varianti495 – 4951S → F in DD. 1 Publication
VAR_008622
Natural varianti560 – 5601C → R in DD; neuropsychiatric phenotype. 1 Publication
VAR_008623
Natural varianti602 – 6021P → L in AKV; loss of activity. 1 Publication
VAR_017532
Natural varianti675 – 6751F → S in DD; multiple neuropsychiatric features.
VAR_008624
Natural varianti683 – 6831K → E in DD; depression.
VAR_008625
Natural varianti702 – 7021D → N in DD; moderate form.
VAR_008626
Natural varianti745 – 7451A → D in DD; moderate form.
VAR_008627
Natural varianti749 – 7491G → R in DD. 1 Publication
VAR_009509
Natural varianti754 – 7541Missing in DD.
VAR_008628
Natural varianti765 – 7651S → L in DD. 1 Publication
VAR_008629
Natural varianti767 – 7671N → S in DD; haemorrhagic lesions and neuropsychiatric phenotype.
VAR_008630
Natural varianti769 – 7691G → R in DD.
VAR_008631
Natural varianti803 – 8031A → T in DD; mild/moderate form.
VAR_008632
Natural varianti838 – 8381A → P in DD; severe form; petit mal epilepsy.
VAR_008633
Natural varianti843 – 8431V → F in DD; depression.
VAR_008634
Natural varianti875 – 8751C → G in DD; retinitis pigmentosa.
VAR_008635
Natural varianti920 – 9201S → Y in DD; mild/moderate/severe form; one patient with epilepsy.
VAR_008636
Natural varianti943 – 9431H → R in DD; learning difficulties.
VAR_008637
Natural varianti975 – 9751P → R in DD.
VAR_008638

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei155 – 18127Missing in isoform 4. 1 PublicationVSP_039392Add
BLAST
Alternative sequencei994 – 104249GKECV…DMFWS → AILE in isoform 2. 1 PublicationVSP_000358Add
BLAST
Alternative sequencei994 – 104249GKECV…DMFWS → VLSSEL in isoform 3. 1 PublicationVSP_039393Add
BLAST
Alternative sequencei994 – 104249GKECV…DMFWS → DIIK in isoform 5. CuratedVSP_039394Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23114 mRNA. Translation: AAA53193.1.
M23116 Genomic DNA. Translation: AAA52757.1.
M23115 mRNA. Translation: AAA53194.1.
M23278, M23116 Genomic DNA. Translation: AAA52758.1.
AC006088 Genomic DNA. No translation available.
BC035588 mRNA. Translation: AAH35588.1.
AK293877 mRNA. Translation: BAG57266.1. Different initiation.
AY186578 mRNA. Translation: AAO47398.1.
CCDSiCCDS9143.1. [P16615-2]
CCDS9144.1. [P16615-1]
PIRiA31981.
B31981.
RefSeqiNP_001672.1. NM_001681.3. [P16615-2]
NP_733765.1. NM_170665.3. [P16615-1]
XP_005253945.1. XM_005253888.1. [P16615-3]
UniGeneiHs.506759.

Genome annotation databases

EnsembliENST00000308664; ENSP00000311186; ENSG00000174437. [P16615-2]
ENST00000539276; ENSP00000440045; ENSG00000174437. [P16615-1]
GeneIDi488.
KEGGihsa:488.
UCSCiuc001tqk.4. human. [P16615-1]
uc001tql.4. human. [P16615-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23114 mRNA. Translation: AAA53193.1.
M23116 Genomic DNA. Translation: AAA52757.1.
M23115 mRNA. Translation: AAA53194.1.
M23278, M23116 Genomic DNA. Translation: AAA52758.1.
AC006088 Genomic DNA. No translation available.
BC035588 mRNA. Translation: AAH35588.1.
AK293877 mRNA. Translation: BAG57266.1. Different initiation.
AY186578 mRNA. Translation: AAO47398.1.
CCDSiCCDS9143.1. [P16615-2]
CCDS9144.1. [P16615-1]
PIRiA31981.
B31981.
RefSeqiNP_001672.1. NM_001681.3. [P16615-2]
NP_733765.1. NM_170665.3. [P16615-1]
XP_005253945.1. XM_005253888.1. [P16615-3]
UniGeneiHs.506759.

3D structure databases

ProteinModelPortaliP16615.
SMRiP16615. Positions 1-992.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106978. 45 interactions.
IntActiP16615. 19 interactions.
MINTiMINT-4991144.
STRINGi9606.ENSP00000440045.

Chemistry

ChEMBLiCHEMBL3901.

Protein family/group databases

TCDBi3.A.3.2.7. the p-type atpase (p-atpase) superfamily.

PTM databases

PhosphoSiteiP16615.

Polymorphism and mutation databases

BioMutaiATP2A2.
DMDMi114312.

Proteomic databases

MaxQBiP16615.
PaxDbiP16615.
PRIDEiP16615.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000308664; ENSP00000311186; ENSG00000174437. [P16615-2]
ENST00000539276; ENSP00000440045; ENSG00000174437. [P16615-1]
GeneIDi488.
KEGGihsa:488.
UCSCiuc001tqk.4. human. [P16615-1]
uc001tql.4. human. [P16615-2]

Organism-specific databases

CTDi488.
GeneCardsiGC12P110719.
HGNCiHGNC:812. ATP2A2.
HPAiHPA062605.
MIMi101900. phenotype.
108740. gene.
124200. phenotype.
neXtProtiNX_P16615.
Orphaneti79151. Acrokeratosis verruciformis of Hopf.
218. Darier disease.
PharmGKBiPA71.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0474.
GeneTreeiENSGT00760000119003.
HOGENOMiHOG000265621.
HOVERGENiHBG105648.
InParanoidiP16615.
KOiK05853.
OMAiPKESRDN.
OrthoDBiEOG73Z2SF.
PhylomeDBiP16615.
TreeFamiTF300651.

Enzyme and pathway databases

ReactomeiREACT_118798. Pre-NOTCH Processing in Golgi.
REACT_23765. Reduction of cytosolic Ca++ levels.
REACT_25149. Ion transport by P-type ATPases.
SignaLinkiP16615.

Miscellaneous databases

ChiTaRSiATP2A2. human.
GenomeRNAii488.
NextBioi2031.
PROiP16615.
SOURCEiSearch...

Gene expression databases

BgeeiP16615.
CleanExiHS_ATP2A2.
ExpressionAtlasiP16615. baseline and differential.
GenevisibleiP16615. HS.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR005782. P-type_ATPase_IIA.
IPR001757. P_typ_ATPase.
IPR030327. SERCA2.
[Graphical view]
PANTHERiPTHR24093:SF234. PTHR24093:SF234. 1 hit.
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
PR00120. HATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01116. ATPase-IIA1_Ca. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of cDNAs from human kidney coding for two alternatively spliced products of the cardiac Ca2+-ATPase gene."
    Lytton J., Maclennan D.H.
    J. Biol. Chem. 263:15024-15031(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
    Tissue: Kidney.
  2. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Eye.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 84-1042 (ISOFORM 4).
    Tissue: Cerebellum.
  5. "Identification of a new SERCA2 splice variant regulated during monocytic differentiation."
    Gelebart P., Martin V., Enouf J., Papp B.
    Biochem. Biophys. Res. Commun. 303:676-684(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 954-1042 (ISOFORM 3), TISSUE SPECIFICITY.
  6. "TRAM2 protein interacts with endoplasmic reticulum Ca2+ pump Serca2b and is necessary for collagen type I synthesis."
    Stefanovic B., Stefanovic L., Schnabl B., Bataller R., Brenner D.A.
    Mol. Cell. Biol. 24:1758-1768(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRAM2.
  7. "Detection of sequence-specific tyrosine nitration of manganese SOD and SERCA in cardiovascular disease and aging."
    Xu S., Ying J., Jiang B., Guo W., Adachi T., Sharov V., Lazar H., Menzoian J., Knyushko T.V., Bigelow D., Schoeneich C., Cohen R.A.
    Am. J. Physiol. 290:H2220-H2227(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NITRATION AT TYR-294 AND TYR-295.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "The anti-apoptotic protein HAX-1 interacts with SERCA2 and regulates its protein levels to promote cell survival."
    Vafiadaki E., Arvanitis D.A., Pagakis S.N., Papalouka V., Sanoudou D., Kontrogianni-Konstantopoulos A., Kranias E.G.
    Mol. Biol. Cell 20:306-318(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HAX1.
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "POST, partner of stromal interaction molecule 1 (STIM1), targets STIM1 to multiple transporters."
    Krapivinsky G., Krapivinsky L., Stotz S.C., Manasian Y., Clapham D.E.
    Proc. Natl. Acad. Sci. U.S.A. 108:19234-19239(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC35G1 AND STIM1.
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580 AND SER-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "Spectrum of novel ATP2A2 mutations in patients with Darier's disease."
    Sakuntabhai A., Burge S., Monk S., Hovnanian A.
    Hum. Mol. Genet. 8:1611-1619(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DD.
  17. "ATP2A2 mutations in Darier's disease: variant cutaneous phenotypes are associated with missense mutations, but neuropsychiatric features are independent of mutation class."
    Ruiz-Perez V.L., Carter S.A., Healy E., Todd C., Rees J.L., Steijlen P.M., Carmichael A.J., Lewis H.M., Hohl D., Itin P., Vahlquist A., Gobello T., Mazzanti C., Reggazini R., Nagy G., Munro C.S., Strachan T.
    Hum. Mol. Genet. 8:1621-1630(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DD, TISSUE SPECIFICITY.
  18. "ATP2A2 mutations in Darier's disease and their relationship to neuropsychiatric phenotypes."
    Jacobsen N.J.O., Lyons I., Hoogendoorn B., Burge S., Kwok P.-Y., O'Donovan M.C., Craddock N., Owen M.J.
    Hum. Mol. Genet. 8:1631-1636(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DD THR-39; ARG-560 AND LEU-765.
  19. Cited for: VARIANTS DD GLU-23; LYS-357; PHE-495 AND ARG-749.
  20. "Acrokeratosis verruciformis of Hopf is caused by mutation in ATP2A2: evidence that it is allelic to Darier's disease."
    Dhitavat J., Macfarlane S., Dode L., Leslie N., Sakuntabhai A., MacSween R., Saihan E., Hovnanian A.
    J. Invest. Dermatol. 120:229-232(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT AKV LEU-602.
  21. "Ca2+-ATPases in non-failing and failing heart: evidence for a novel cardiac sarco/endoplasmic reticulum Ca2+-ATPase 2 isoform (SERCA2c)."
    Dally S., Bredoux R., Corvazier E., Andersen J.P., Clausen J.D., Dode L., Fanchaouy M., Gelebart P., Monceau V., Del Monte F., Gwathmey J.K., Hajjar R., Chaabane C., Bobe R., Raies A., Enouf J.
    Biochem. J. 395:249-258(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  22. "Three-base deletion mutation c.120_122delGTT in ATP2A2 leads to the unique phenotype of comedonal Darier disease."
    Tsuruta D., Akiyama M., Ishida-Yamamoto A., Imanishi H., Mizuno N., Sowa J., Kobayashi H., Ishii M., Kurokawa I., Shimizu H.
    Br. J. Dermatol. 162:687-689(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DD LEU-41 DEL.

Entry informationi

Entry nameiAT2A2_HUMAN
AccessioniPrimary (citable) accession number: P16615
Secondary accession number(s): A6NDN7
, B4DF05, P16614, Q86VJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: June 24, 2015
This is version 185 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.